|Title||Discovery of ubonodin, an antimicrobial lasso peptide active against members of the Burkholderia cepacia complex.|
|Publication Type||Journal Article|
|Year of Publication||2019|
|Authors||Cheung-Lee, WLing, Parry, M, Zong, C, Cartagena, AJaramillo, Darst, S, Connell, N, Russo, R, A Link, J|
|Date Published||2019 Nov 25|
We report the heterologous expression, structure, and antimicrobial activity of a lasso peptide, ubonodin, encoded in the genome of Burkholderia ubonensis . The topology of ubonodin is unprecedented amongst lasso peptides with 18 of its 28 amino acids found in the mechanically-bonded loop segment. Ubonodin inhibits RNA polymerase in vitro and has potent antimicrobial activity against several pathogenic members of the Burkholderia genus, most notably B. cepacia and B. multivorans , causative agents of lung infections in cystic fibrosis patients.